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Database: UniProt
Entry: A0A1E3ING6_9TREE
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ID   A0A1E3ING6_9TREE        Unreviewed;       248 AA.
AC   A0A1E3ING6;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   16-JAN-2019, entry version 8.
DE   RecName: Full=Protein-lysine N-methyltransferase EFM6 {ECO:0000256|HAMAP-Rule:MF_03198};
DE            EC=2.1.1.- {ECO:0000256|HAMAP-Rule:MF_03198};
DE   AltName: Full=Elongation factor methyltransferase 6 {ECO:0000256|HAMAP-Rule:MF_03198};
GN   Name=EFM6 {ECO:0000256|HAMAP-Rule:MF_03198};
GN   ORFNames=L203_01998 {ECO:0000313|EMBL:ODN90078.1};
OS   Cryptococcus depauperatus CBS 7841.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Tremellomycetes; Tremellales; Cryptococcaceae; Cryptococcus.
OX   NCBI_TaxID=1295531 {ECO:0000313|EMBL:ODN90078.1, ECO:0000313|Proteomes:UP000094043};
RN   [1] {ECO:0000313|EMBL:ODN90078.1, ECO:0000313|Proteomes:UP000094043}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 7841 {ECO:0000313|EMBL:ODN90078.1,
RC   ECO:0000313|Proteomes:UP000094043};
RA   Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA   Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S.,
RA   Birren B.;
RT   "Evolution of pathogenesis and genome organization in the
RT   Tremellales.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: S-adenosyl-L-methionine-dependent protein-lysine N-
CC       methyltransferase that methylates elongation factor 1-alpha.
CC       {ECO:0000256|HAMAP-Rule:MF_03198}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03198}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding
CC       methyltransferase superfamily. METTL21 family. EFM6 subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_03198}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:ODN90078.1}.
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DR   EMBL; AWGK01000007; ODN90078.1; -; Genomic_DNA.
DR   OrthoDB; 1494909at2759; -.
DR   Proteomes; UP000094043; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_03198; Methyltr_EFM6; 1.
DR   InterPro; IPR033684; EFM6.
DR   InterPro; IPR019410; Methyltransf_16.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   Pfam; PF10294; Methyltransf_16; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000094043};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03198};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_03198};
KW   Reference proteome {ECO:0000313|Proteomes:UP000094043};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_03198};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_03198}.
FT   REGION       97     99       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_03198}.
FT   BINDING      67     67       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_03198}.
FT   BINDING     120    120       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_03198}.
FT   BINDING     151    151       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_03198}.
FT   BINDING     170    170       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_03198}.
SQ   SEQUENCE   248 AA;  27569 MW;  9F9C2F01D80F53EB CRC64;
     MSDAPEQARS RSSSISTVSS ALPTFEALVP PRIGLTSEEK ETRIDVPGLK DIKLKIDAGP
     GCGGIAWPSG EVLSRYLAYR HAIDPTRLYG QKVIELGSGT GLVGIVAAML EPTAEIWVTD
     QAQLLELMTT NAELNLKGKN QRNVHVAELN WGEPLPSNIP TEEASLILAA DCVYFEPTFP
     LLVKTLCDLA PVGKPMEILF CYKKRRKADK RFFIMLKKHF TLTPVDDDKD SERYQREGVT
     LMKLKRRK
//
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